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Anti-GalNAc-T2 [UH4] monoclonal antibody

Invented by Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen, at University of Copenhagen Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel at University of Copenhagen

Info

Applications ELISA IHC IF IP
Antigen/Gene or Protein Targets GalNAc-T2/GALNT2
Synonyms UH4, 4C4
Reactivity Human
Relevance GalNAc-T2 is one of many polypeptide GalNAc-transferases that
attach GalNAc to proteins forming the GalNAc1-O-Ser/Thr
linkage for GalNAc-type O-glycosylation. The GalNAc-transferase
isoforms have considerably overlapping functions as well as
unique distinct functions. GalNAc-T1 and -T2 are the main
contributors to O-glycosylation of peptides in most cells and they
have distinct functions as shown in murine models. GalNAc-T2
has been implicated in lipoprotein metabolism and risk of
atherosclerosis as well as cancer.
O-glycans are important biomarkers in cancer. The truncated
O-glycans comprising Tn formed by the GalNAc transferases and
T formed by further elongation by the core1 synthase (C1GalT1)
are widely recognized as pancarcinoma antigens. They are
masked by sialic acid or further elongation or branching in
normal cells.

Validation:
1. Positive reaction (IC/IF) in cells expressing GalNAc-T2
using close isoforms as negative controls e.g. GalNAc –T7/ –T10.
2. Selective IP of active GalNAc-T2 from total cell extracts.
3. Distinct perinuclear staining in cell lines (ICC/IF) and tissues
(IHC, IF) suggestive of Golgi localization.
4. Loss of staining (IC/IF) following KO of GalNAc-T2
Host Mouse
Immunogen Catalytically active secreted GalNAc-T2 produced in insect cells. Recombinant protein containing aa. 52-571 (Uniprot isoform-1)
Immunogen UniProt ID Q10471
Subclass IgG1
Strain Balb/c
Notes UH4 4C4 can be used to probe subcellular topology of active GalNAc-T2 in cells and tissues as well as its presence in body fluids.

UH4 4C4 tolerates fixation in ice-cold acetone and paraformaldehyde (but not methanol). UH4 4C4 does not tolerate routine FFPE methods used for histopathological archives. Incubation time is usually 2 hrs or ON.

Reactivity can be easily tested by IC on air-dried, acetone fixed cells i.e. air-dry cells in PBS on multi-well slides and fix in ice-cold acetone for 8-10 min followed by drying and incubation with primary antibody.
Research Area Cancer, Cell Structure and Motility, Fluorescent Cell Imaging, Structural Biology

References

There are 8 reference entries for this reagent.

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References: 8 entries

A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.

Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.

Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.

Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.

Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.

Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.

Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.

Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.


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References: 8 entries

A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.

Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.

Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.

Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.

Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.

Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.

Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.

Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.


Add a reference

Inventor Information

Inventors

Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen

Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen

Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel

Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel

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